Cooperative interactions between the central spindle and the contractile ring during Drosophila cytokinesis.
We analyzed male meiosis in mutants of the chickadee (chic) locus, a Drosophila melanogaster gene that encodes profilin, a low molecular weight actin-binding protein that modulates F-actin polymerization. These mutants are severely defective in meiotic cytokinesis. During ana-telophase of both meiotic divisions, they exhibit a central spindle less dense than wild type; certain chic allelic combinations cause almost complete disappearance of the central spindle. Moreover, chic mutant spermatocytes fail to form an actomyosin contractile ring. To further investigate the relationships between the central spindle and the contractile ring, we examined meiosis in the cytokinesis-defective mutants KLP3A and diaphanous and in testes treated with cytochalasin B. In all cases, we found that the central spindle and the contractile ring in meiotic ana-telophases were simultaneously absent. Together, these results suggest a cooperative interaction between elements of the actin-based contractile ring and the central spindle microtubules: When one of these structures is disrupted, the proper assembly of the other is also affected. In addition to effects on the central spindle and the cytokinetic apparatus, we observed another consequence of chic mutations: A large fraction of chic spermatocytes exhibit abnormal positioning and delayed migration of asters to the cell poles. A similar phenotype was seen in testes treated with cytochalasin B and has been noted previously in mutants at the twinstar locus, a gene that encodes a Drosophila member of the cofilin/ADF family of actin-severing proteins. These observations all indicate that proper actin assembly is necessary for centrosome separation and migration.
Giansanti
M G
MG
Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Genetica e Biologia Molecolare, Universitá di Roma "La Sapienza," 00185 Rome, Italy.
Bonaccorsi
S
S
Williams
B
B
Williams
E V
EV
Santolamazza
C
C
Goldberg
M L
ML
Gatti
M
M
D000199:Actins / Q000378:metabolism; D000705:Anaphase / Q000502:physiology; D000818:Animals; D001483:Base Sequence; D002455:Cell Division / Q000502:physiology*; D018385:Centrosome / Q000378:metabolism*; D003285:Contractile Proteins / Q000378:metabolism*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000502:physiology; D004843:Epistasis, Genetic; D017344:Genes, Insect / Q000235:genetics; D008297:Male; D008540:Meiosis / Q000502:physiology; D008840:Microfilament Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D008870:Microtubules / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics / Q000502:physiology; D051304:Profilins; D013091:Spermatogenesis / Q000502:physiology; D008941:Spindle Apparatus / Q000378:metabolism*; D013692:Telophase / Q000502:physiology; D013997:Time Factors
D000199:Actins; D003285:Contractile Proteins; D029721:Drosophila Proteins; D008840:Microfilament Proteins; D051304:Profilins; C495737:chic protein, Drosophila; C097180:tsr protein, Drosophila